The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome β-type subunit

Kerrie A. Smyth, John M. Belote

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

Proteasomes are multicatalytic complexes that function as the major proteolytic machinery in regulated protein degradation. The eukaryotic 20S proteasome proteolytic core structure comprises 14 different subunits: 7 α- type and 7 β-type. DTS7 is a dominant temperature-sensitive (DTS) lethal mutation at 29°that also acts as a recessive lethal at ambient temperatures. DTS7 maps to cytological position 71AB. Molecular characterization of DTS7 reveals that this is caused by a missense mutation in a β-type subunit gene, β2. A previously characterized DTS mutant, l(3)73Ai1, results from a missense mutation in another β-type subunit gene, β6. These two mutants share a very similar phenotype, show a strong allele- specific genetic interaction, and are rescued by the same extragenic suppressor, Su(DTS)-1. We propose that these mutants might act as 'poison subunits,' disrupting proteasome function in a dosage-dependent manner, and suggest how they may interact on the basis of the structure of the yeast 20S proteasome.

Original languageEnglish (US)
Pages (from-to)211-220
Number of pages10
JournalGenetics
Volume151
Issue number1
StatePublished - Jan 1 1999

ASJC Scopus subject areas

  • Genetics

Fingerprint Dive into the research topics of 'The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome β-type subunit'. Together they form a unique fingerprint.

  • Cite this